Residue-by-residue listing for refined_10 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - - -62.2 180.1 - - - - - - 181.1 - 33.3 - 2 GLY 2 - - - - - - - - - - - 181.2 - - - 3 HIS 3 B - - -64.3 - - - - - - - 179.7 - 33.9 - 4 HIS 4 B 54.8 - - - - - - - - - 180.2 -.7 32.2 - +* +* 5 HIS 5 B - - -68.5 - - - - - - - 172.1 - 33.8 - * * 6 HIS 6 b - 188.1 - - - - - - - - 179.7 -.9 31.0 - +* +* 7 HIS 7 b - 179.5 - - - - - - - - 177.7 - 34.3 - 8 HIS 8 B - - -71.2 - - - - - - - 175.4 - 34.8 - 9 LEU 9 b - - -66.8 - - - - - - - 180.8 - 31.2 - 10 GLU 10 b - - -55.9 174.6 - - - - - - 182.5 -1.8 34.5 - 11 MET 11 B 63.1 - - - - - - - - - 177.4 -1.3 33.5 - 12 ALA 12 b - - - - - - - - - - 181.2 - 34.0 - 13 SER 13 B - - -53.1 - - - - - - - 182.5 -.8 35.1 - +* +* 14 GLU 14 B 52.7 - - - - - - - - - 176.9 - 30.3 - * * 15 GLU 15 B 41.9 - - - - - - - - - 177.4 -.8 31.6 - * +* +* 16 GLY 16 S - - - - - - - - - - - 179.6 -1.6 - - 17 GLN 17 B 54.4 - - 181.2 - - - - - - 180.0 -.5 29.9 - ** * ** 18 VAL 18 B 63.3 - - - - - - - - - 182.1 - 35.8 - 19 ILE 19 E B - - -60.9 - - - - - - - 178.1 -3.0 31.6 - * * Residue-by-residue listing for refined_10 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 ALA 20 E B - - - - - - - - - - 180.8 -.8 34.0 - +* +* 21 CYS 21 E B - - -55.2 - - - - - - - 177.2 -1.6 35.3 - 22 HIS 22 S A - - -61.8 - - - - - - - 181.3 - 33.9 - 23 THR 23 h B 55.2 - - - - - - - - - 175.9 - 35.9 - 24 VAL 24 H A - 182.5 - - - -74.8 -25.0 - - - 179.9 - 34.3 - * * 25 GLU 25 H A - 188.0 - - - -61.3 -51.1 - - - 176.4 - 35.4 - * * 26 THR 26 H A - - -59.5 - - -61.0 -46.1 - - - 178.5 - 34.7 - 27 TRP 27 H A - 171.2 - - - -53.8 -50.7 - - - 180.9 -1.6 35.1 - 28 ASN 28 H A - 186.4 - - - -60.7 -43.0 - - - 180.3 -3.3 35.2 - +* +* 29 GLU 29 H A - 181.4 - 180.2 - -66.2 -42.2 - - - 181.9 -2.2 34.0 - 30 GLN 30 H A - - -69.2 - - -67.3 -36.5 - - - 176.4 -2.9 32.7 - * * 31 LEU 31 H A - - -66.0 180.6 - -64.9 -45.2 - - - 176.4 -2.2 34.4 - 32 GLN 32 H A - 182.4 - 179.0 - -63.0 -37.7 - - - 177.7 -1.9 32.9 - 33 LYS 33 H A - 177.0 - - - -56.4 -43.1 - - - 179.4 -2.5 34.2 - 34 ALA 34 H A - - - - - -71.8 -48.6 - - - 182.6 -2.1 33.9 - 35 ASN 35 H A - 188.3 - - - -58.7 -52.8 - - - 182.5 -3.0 36.6 - * * * 36 GLU 36 H A - 189.4 - - - -59.7 -31.3 - - - 183.1 -3.5 35.6 - ** ** 37 SER 37 h A - - -54.5 - - - - - - - 183.7 -1.0 36.1 - * * 38 LYS 38 T l - 187.6 - 179.1 - - - - - - 179.2 -1.7 29.5 - * * 39 THR 39 t B - - -45.2 - - - - - - - 180.7 -2.6 35.5 - * * 40 LEU 40 e B 58.9 - - - - - - - - - 184.1 - 33.7 - 41 VAL 41 E B 59.1 - - - - - - - - - 178.3 - 33.2 - 42 VAL 42 E B - 181.6 - - - - - - - - 184.8 -2.9 34.3 - * * 43 VAL 43 E B - 184.6 - - - - - - - - 179.0 -3.2 34.2 - * * 44 ASP 44 E B - 175.0 - - - - - - - - 175.2 -3.2 36.7 - +* +* 45 PHE 45 E B - - -64.0 - - - - - - - 184.8 -2.3 35.7 - 46 THR 46 E B - 186.5 - - - - - - - - 177.8 -2.5 36.0 - 47 ALA 47 t B - - - - - - - - - - 183.3 - 34.3 - 48 SER 48 T A - 187.9 - - - - - - - - 178.8 - 33.6 - 49 TRP 49 T A 50.2 - - - - - - - - - 177.8 - 30.4 - 50 CYS 50 h B - 172.8 - 220.3 - - - 51.1 - 2.0 183.2 -2.5 33.7 - ** *** *** 51 GLY 51 H - - - - - - -53.6 -71.9 - - - 181.9 -.6 - - +** +* +** 52 PRO 52 H - - - - - -60.8 -60.8 -33.5 - - - 179.9 - 38.3 - * * 53 CYS 53 H A - - -53.2 - - -63.1 -36.7 51.1 - 2.0 180.6 - 36.7 - *** *** 54 ARG 54 H A - 180.1 - 175.6 - -78.1 -31.1 - - - 177.0 -1.9 33.5 - * * 55 PHE 55 H A - 179.1 - - - -69.3 -14.5 - - - 179.1 -1.7 33.0 - ** ** 56 ILE 56 H A - - -63.5 - - -85.6 -13.4 - - - 176.4 -.7 33.4 - +* ** +* ** Residue-by-residue listing for refined_10 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 ALA 57 H A - - - - - -59.6 -52.3 - - - 175.6 -1.4 30.7 - * * 58 PRO 58 H - - - - - -64.8 -64.8 -31.9 - - - 182.9 - 39.0 - * * 59 PHE 59 H A - 192.9 - - - -68.2 -42.9 - - - 178.2 -.8 35.3 - +* +* 60 PHE 60 H A - 190.6 - - - -73.7 -32.1 - - - 176.4 -3.1 34.2 - * * 61 ALA 61 H A - - - - - -66.2 -34.8 - - - 174.9 -1.9 33.5 - 62 ASP 62 H A - 178.0 - - - -59.8 -44.2 - - - 176.1 -1.9 36.1 - 63 LEU 63 H A - - -64.5 181.9 - -58.3 -44.8 - - - 176.8 -1.3 34.9 - * * 64 ALA 64 H A - - - - - -64.3 -31.2 - - - 177.3 -2.0 33.7 - 65 LYS 65 H A - 177.7 - 183.6 - -69.3 -33.8 - - - 181.8 -1.6 35.4 - 66 LYS 66 H A - - -59.1 180.8 - -77.1 -37.7 - - - 180.8 -1.6 32.8 - 67 LEU 67 h B - - -66.8 171.1 - - - - - - 181.3 -1.9 33.3 - 68 PRO 68 S - - - - - -69.4 - - - - - 186.0 - 39.2 - * +* +* 69 ASN 69 S A - - -62.2 - - - - - - - 181.8 - 34.2 - 70 VAL 70 S B - 178.9 - - - - - - - - 181.7 - 33.8 - 71 LEU 71 E B - - -67.5 - - - - - - - 176.6 -1.0 34.8 - * * 72 PHE 72 E B - - -62.2 - - - - - - - 184.4 -.6 34.3 - +* +* 73 LEU 73 E B - - -73.2 161.5 - - - - - - 176.2 -2.3 34.6 - 74 LYS 74 E B - - -71.3 - - - - - - - 177.1 -2.3 35.8 - 75 VAL 75 E B - 177.9 - - - - - - - - 177.1 -3.3 34.7 - +* +* 76 ASP 76 E B - 185.6 - - - - - - - - 186.1 -.6 33.6 - * +* +* 77 THR 77 e A 52.5 - - - - - - - - - 176.4 -3.1 32.7 - * * 78 ASP 78 T A - 188.7 - - - - - - - - 179.2 - 34.5 - 79 GLU 79 T a - - -64.9 - - - - - - - 179.4 - 36.2 - 80 LEU 80 h b - - -67.7 180.0 - - - - - - 184.4 -3.5 33.9 - ** ** 81 LYS 81 H A - 192.4 - 181.9 - -68.5 -34.6 - - - 177.5 -1.2 34.8 - * * 82 SER 82 H A - - -58.1 - - -67.3 -31.2 - - - 178.6 - 33.7 - 83 VAL 83 H A - 179.4 - - - -73.0 -36.7 - - - 176.7 - 33.8 - 84 ALA 84 H A - - - - - -59.0 -43.9 - - - 178.1 -1.8 34.3 - 85 SER 85 H A - - -54.5 - - -68.2 -38.6 - - - 182.0 -1.8 35.3 - 86 ASP 86 H A - 181.3 - - - -61.4 -36.2 - - - 179.9 -2.0 34.3 - 87 TRP 87 h A - - -65.1 - - - - - - - 176.3 -2.0 31.6 - 88 ALA 88 T L - - - - - - - - - - 178.4 -1.4 33.5 - 89 ILE 89 t B - - -57.5 - - - - - - - 182.9 -3.0 33.8 - * * 90 GLN 90 A - 180.8 - 183.2 - - - - - - 181.7 -.9 35.2 - * * 91 ALA 91 S B - - - - - - - - - - 180.2 - 33.7 - 92 MET 92 S B - - -58.3 175.1 - - - - - - .7 - 35.1 - 93 PRO 93 e cis - - - - - -91.2 - - - - - 174.5 - 39.7 - ** +* ** 94 THR 94 E B - - -63.0 - - - - - - - 180.1 -1.9 33.7 - 95 PHE 95 E B - - -49.2 - - - - - - - 185.3 -2.8 37.2 - * * * Residue-by-residue listing for refined_10 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 96 MET 96 E B - 186.8 - 173.9 - - - - - - 182.2 -3.3 32.0 - +* +* 97 PHE 97 E B - - -65.6 - - - - - - - 182.1 -2.9 36.9 - * * 98 LEU 98 E B - - -53.8 179.5 - - - - - - 171.4 -2.3 36.7 - * * 99 LYS 99 E B - 170.0 - 174.3 - - - - - - 180.4 -2.8 32.9 - 100 GLU 100 T l - - -66.7 - - - - - - - 182.6 - 33.5 - 101 GLY 101 T - - - - - - - - - - - 178.1 - - - 102 LYS 102 E B - - -61.2 178.4 - - - - - - 185.5 -2.4 34.5 - 103 ILE 103 E B - - -57.9 177.7 - - - - - - 175.2 - 33.5 - 104 LEU 104 E a - - -67.7 184.8 - - - - - - 183.4 -2.0 34.5 - 105 ASP 105 E B - - -62.0 - - - - - - - 174.5 -2.6 35.0 - 106 LYS 106 E B 59.2 - - 174.6 - - - - - - 181.1 - 32.2 - 107 VAL 107 E B - 180.1 - - - - - - - - 180.5 -3.0 34.6 - * * 108 VAL 108 E B 58.3 - - - - - - - - - 181.4 -.5 33.2 - ** ** 109 GLY 109 e - - - - - - - - - - - 181.7 -3.0 - - * * 110 ALA 110 B - - - - - - - - - - 175.9 - 33.8 - 111 LYS 111 h B - - -66.6 - - - - - - - 182.6 -.9 34.2 - * * 112 LYS 112 H A - - -61.4 173.9 - -69.8 -50.8 - - - 182.8 -.5 35.8 - * ** ** 113 ASP 113 H A - 178.3 - - - -69.3 -47.0 - - - 180.9 - 34.0 - 114 GLU 114 H A - 183.2 - 174.1 - -64.8 -32.9 - - - 178.2 - 32.4 - 115 LEU 115 H A - 188.9 - - - -62.7 -46.9 - - - 176.4 -1.4 35.1 - 116 GLN 116 H A - - -66.8 - - -55.9 -40.6 - - - 179.9 -1.8 34.2 - 117 SER 117 H A - 182.3 - - - -68.3 -34.5 - - - 178.4 -1.9 33.7 - 118 THR 118 H A - - -52.2 - - -69.6 -35.0 - - - 176.7 -2.2 34.7 - 119 ILE 119 H A - - -56.4 - - -63.9 -51.3 - - - 180.1 -2.2 34.8 - * * 120 ALA 120 H A - - - - - -60.3 -31.3 - - - 176.2 -2.7 33.0 - 121 LYS 121 H A - 186.1 - 181.3 - -59.7 -44.0 - - - 180.1 -1.7 36.1 - 122 HIS 122 H A - - -75.3 - - -75.6 -35.1 - - - 179.8 -1.5 32.9 - 123 LEU 123 h b - - -84.2 - - - - - - - 180.4 -2.2 32.2 - * * 124 ALA 124 - - - - - - - - - - - - -1.5 34.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * ** ** +* +** *** * ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 55.7 182.7 -62.4 179.4 -71.6 -65.4 -39.4 51.1 - 2.0 179.6 -2.0 34.2 *** *** Standard deviations: 5.8 5.6 7.1 9.3 13.6 6.7 10.1 .0 - .0 2.9 .8 1.7 Numbers of values: 13 40 49 28 4 46 46 2 0 2 122 84 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_10 Page 5 ---------------------------------------- KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_10 Page 6 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - 1.238 1.504 1.539 1.460 - 115.32 121.08 110.57 109.66 111.88 123.58 2 GLY 2 1.301 1.231 1.495 - 1.427 122.42 116.74 120.32 - 109.74 - 122.91 +* * * * +* 3 HIS 3 1.299 1.230 1.502 1.532 1.447 121.33 116.47 120.64 109.92 110.36 111.44 122.89 ** * ** 4 HIS 4 1.299 1.231 1.513 1.552 1.449 121.26 116.37 120.65 111.92 110.90 111.87 122.98 ** * ** 5 HIS 5 1.310 1.242 1.508 1.542 1.452 121.66 116.09 120.83 108.79 111.63 112.40 123.05 * * * 6 HIS 6 1.304 1.232 1.509 1.543 1.434 121.59 114.01 121.99 111.92 108.57 114.34 123.82 +* * * ** ** 7 HIS 7 1.300 1.227 1.523 1.549 1.429 123.66 115.96 120.73 111.35 108.52 110.26 123.15 ** +* * ** 8 HIS 8 1.315 1.234 1.489 1.551 1.455 121.80 116.93 120.18 107.74 109.12 113.02 122.88 +* * * * +* 9 LEU 9 1.304 1.247 1.508 1.551 1.435 120.42 114.35 121.86 111.53 109.27 114.23 123.63 +* * * ** ** 10 GLU 10 1.308 1.239 1.502 1.533 1.423 122.74 115.20 121.26 111.60 107.87 109.94 123.38 +* * +* * +* 11 MET 11 1.301 1.234 1.503 1.547 1.429 122.13 115.65 120.93 110.56 110.53 111.57 123.41 ** * +* ** Residue-by-residue listing for refined_10 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 ALA 12 1.291 1.246 1.507 1.516 1.427 121.93 115.51 121.02 110.90 108.61 110.90 123.41 +** +* +** 13 SER 13 1.302 1.243 1.535 1.522 1.441 122.36 117.59 119.84 111.40 109.39 108.25 122.56 +* * +* 14 GLU 14 1.323 1.229 1.529 1.548 1.422 121.20 114.86 121.69 112.31 112.98 113.08 123.40 +* * +* +* 15 GLU 15 1.309 1.242 1.513 1.557 1.435 122.97 115.97 120.96 112.25 111.25 112.25 123.01 * * * * * * 16 GLY 16 1.305 1.232 1.501 - 1.444 120.65 116.67 120.82 - 112.63 - 122.51 +* +* 17 GLN 17 1.307 1.232 1.480 1.513 1.421 120.30 112.52 122.50 112.04 113.22 113.70 124.94 +* ** +* +* * * +* * ** 18 VAL 18 1.264 1.241 1.523 1.543 1.408 125.15 118.77 119.26 111.39 107.43 108.29 121.88 *4.6* +** +* * * * +* *4.6* 19 ILE 19 1.315 1.232 1.524 1.566 1.434 118.52 116.50 121.04 110.99 110.01 114.00 122.39 * * +* * +* 20 ALA 20 1.305 1.234 1.508 1.524 1.441 121.13 116.51 120.65 110.57 109.26 110.99 122.83 +* +* 21 CYS 21 1.299 1.226 1.509 1.510 1.418 121.11 116.34 120.77 109.69 109.63 109.84 122.86 ** ** ** 22 HIS 22 1.297 1.221 1.509 1.543 1.446 121.42 115.38 121.35 110.52 109.13 111.31 123.27 ** ** 23 THR 23 1.321 1.247 1.513 1.555 1.444 122.98 116.26 120.45 107.47 108.93 111.68 123.29 24 VAL 24 1.316 1.213 1.531 1.554 1.446 121.81 115.59 121.29 109.99 108.66 111.51 123.08 25 GLU 25 1.331 1.246 1.546 1.535 1.461 123.15 115.99 120.84 110.34 109.76 108.72 123.16 * * * 26 THR 26 1.339 1.231 1.529 1.545 1.458 122.19 115.39 120.74 109.71 109.94 110.60 123.85 27 TRP 27 1.323 1.238 1.534 1.538 1.456 123.57 115.21 121.30 111.14 111.14 108.12 123.45 * * * 28 ASN 28 1.311 1.243 1.525 1.533 1.453 123.62 115.89 120.94 110.38 110.49 109.02 123.15 * * * 29 GLU 29 1.329 1.225 1.525 1.535 1.454 122.12 116.60 120.41 109.81 110.93 111.06 122.98 30 GLN 30 1.324 1.233 1.514 1.486 1.423 122.57 117.30 120.28 111.22 113.57 110.29 122.42 ** +* ** 31 LEU 31 1.314 1.237 1.503 1.487 1.412 121.14 116.01 120.59 110.60 110.31 109.75 123.40 * * ** ** ** 32 GLN 32 1.323 1.204 1.518 1.527 1.432 120.66 116.43 120.34 110.72 109.37 112.40 123.20 * * * * 33 LYS 33 1.329 1.235 1.528 1.548 1.459 122.82 116.90 120.25 110.55 110.24 110.45 122.83 34 ALA 34 1.331 1.234 1.529 1.520 1.447 120.39 115.37 121.06 110.83 110.35 110.30 123.52 35 ASN 35 1.321 1.236 1.518 1.524 1.474 124.04 114.27 121.90 108.45 111.18 108.45 123.83 * * * 36 GLU 36 1.301 1.226 1.537 1.533 1.469 124.31 116.77 120.66 108.88 111.51 109.44 122.57 ** * ** 37 SER 37 1.315 1.244 1.522 1.507 1.441 121.53 116.07 120.22 109.16 111.48 108.47 123.71 * * * * 38 LYS 38 1.332 1.246 1.534 1.515 1.411 124.05 114.22 122.48 114.37 110.84 112.79 123.02 ** * ** * ** 39 THR 39 1.313 1.236 1.525 1.523 1.420 122.84 115.38 121.48 108.42 108.50 111.06 123.14 * ** ** 40 LEU 40 1.277 1.240 1.526 1.526 1.383 123.97 116.15 120.84 113.57 109.31 108.70 122.94 +*** +*** * +* * +*** 41 VAL 41 1.281 1.237 1.537 1.565 1.441 121.58 116.03 121.07 111.36 111.21 111.01 122.87 *** * *** Residue-by-residue listing for refined_10 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.311 1.239 1.516 1.536 1.442 122.27 116.59 120.65 109.67 108.69 111.70 122.76 * * 43 VAL 43 1.308 1.232 1.523 1.542 1.439 120.96 115.08 121.24 109.41 111.58 111.22 123.68 +* +* 44 ASP 44 1.296 1.238 1.528 1.534 1.450 124.40 117.10 120.06 109.77 109.31 107.70 122.76 ** +* +* ** 45 PHE 45 1.324 1.241 1.508 1.524 1.438 121.90 116.67 120.41 108.71 108.16 110.60 122.89 * * * 46 THR 46 1.294 1.223 1.525 1.561 1.430 120.92 116.34 120.50 109.92 109.41 109.07 123.16 ** * * ** 47 ALA 47 1.304 1.241 1.510 1.520 1.432 122.58 116.41 120.11 110.93 108.13 110.43 123.48 +* * * +* 48 SER 48 1.321 1.230 1.545 1.539 1.464 123.35 117.21 120.51 110.82 112.51 110.00 122.28 49 TRP 49 1.329 1.235 1.535 1.549 1.454 121.23 116.86 120.65 112.30 113.23 112.62 122.50 * * * 50 CYS 50 1.311 1.223 1.525 1.533 1.449 121.99 116.21 120.12 110.95 109.95 110.74 123.67 * * 51 GLY 51 1.336 1.235 1.535 - 1.471 122.60 118.95 119.78 - 114.77 - 121.26 * * * * * * 52 PRO 52 1.355 1.216 1.523 1.538 1.474 122.45 115.61 121.04 110.48 111.98 103.91 123.32 53 CYS 53 1.317 1.230 1.528 1.516 1.456 123.59 115.79 121.17 108.63 110.17 108.35 123.04 * * * 54 ARG 54 1.316 1.225 1.524 1.520 1.442 122.37 116.42 120.88 112.06 110.58 109.56 122.65 * * 55 PHE 55 1.327 1.235 1.539 1.543 1.467 121.89 115.67 121.83 111.33 110.38 111.13 122.44 56 ILE 56 1.305 1.220 1.534 1.548 1.429 121.64 116.85 121.17 111.92 109.84 110.55 121.85 +* +* * +* 57 ALA 57 1.332 1.233 1.556 1.534 1.457 120.65 120.20 119.33 112.48 111.38 112.63 120.46 * ** * * +* ** 58 PRO 58 1.374 1.229 1.538 1.540 1.472 121.55 115.90 120.96 109.56 111.35 103.93 123.10 ** ** 59 PHE 59 1.329 1.231 1.543 1.540 1.463 122.78 115.33 121.46 110.86 109.77 108.50 123.22 * * 60 PHE 60 1.315 1.225 1.536 1.538 1.461 123.82 116.42 121.10 112.10 109.68 108.96 122.47 * * * 61 ALA 61 1.325 1.227 1.529 1.515 1.462 121.37 115.55 121.03 110.77 109.83 110.87 123.42 62 ASP 62 1.327 1.222 1.503 1.510 1.471 123.37 114.47 121.64 108.88 109.42 109.13 123.89 * * 63 LEU 63 1.298 1.237 1.546 1.524 1.435 123.77 115.99 120.91 111.59 110.88 107.99 123.07 ** * * * ** 64 ALA 64 1.324 1.227 1.536 1.523 1.467 122.98 115.47 121.74 110.73 110.72 110.38 122.73 65 LYS 65 1.311 1.231 1.524 1.520 1.450 123.33 116.15 120.95 110.49 110.66 108.34 122.89 * * * 66 LYS 66 1.314 1.233 1.523 1.532 1.450 121.29 117.27 120.16 111.05 111.82 111.22 122.56 * * 67 LEU 67 1.319 1.220 1.527 1.507 1.436 121.59 116.74 120.87 111.48 112.51 109.70 122.38 * * * 68 PRO 68 1.342 1.237 1.539 1.538 1.476 123.05 116.53 120.67 109.23 113.95 103.48 122.80 69 ASN 69 1.337 1.230 1.511 1.530 1.454 122.18 116.19 120.67 109.38 112.06 110.88 123.13 70 VAL 70 1.308 1.233 1.519 1.554 1.444 122.27 116.32 120.78 110.58 109.66 111.39 122.89 +* +* 71 LEU 71 1.311 1.239 1.510 1.546 1.419 121.81 115.49 121.13 109.54 109.97 111.03 123.35 * ** ** 72 PHE 72 1.301 1.238 1.510 1.527 1.433 122.22 116.24 120.60 109.72 108.21 111.73 123.15 +* * * +* Residue-by-residue listing for refined_10 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 73 LEU 73 1.291 1.224 1.506 1.519 1.447 122.35 115.50 120.96 110.50 112.66 109.09 123.53 +** +** 74 LYS 74 1.313 1.241 1.502 1.519 1.417 123.35 115.99 120.63 109.25 109.32 109.84 123.36 * * ** ** 75 VAL 75 1.293 1.237 1.506 1.559 1.428 121.82 116.17 120.80 109.51 108.56 111.67 123.02 +** +* +** 76 ASP 76 1.305 1.228 1.500 1.511 1.433 120.42 115.98 120.61 110.82 107.40 111.73 123.38 +* * * * +* 77 THR 77 1.291 1.235 1.529 1.529 1.435 123.08 117.78 120.13 111.28 114.13 110.34 122.08 +** * * +** 78 ASP 78 1.316 1.236 1.509 1.524 1.451 119.91 113.69 122.14 109.99 107.42 111.25 124.15 * * * 79 GLU 79 1.312 1.231 1.521 1.514 1.428 124.75 116.18 121.18 109.38 110.53 108.42 122.64 * +* +* * +* 80 LEU 80 1.311 1.237 1.508 1.512 1.406 122.68 113.72 122.40 112.01 109.05 109.84 123.87 * +** * * +** 81 LYS 81 1.298 1.232 1.533 1.525 1.427 123.78 116.27 121.05 111.79 110.20 108.34 122.66 ** +* * * ** 82 SER 82 1.324 1.234 1.537 1.520 1.449 121.55 116.01 120.98 111.39 110.67 109.94 122.95 83 VAL 83 1.332 1.233 1.530 1.559 1.457 122.46 115.89 121.15 110.60 109.50 111.30 122.94 84 ALA 84 1.330 1.234 1.528 1.519 1.460 122.16 115.63 121.29 110.22 109.94 110.36 123.06 85 SER 85 1.320 1.240 1.549 1.529 1.445 122.29 115.75 121.17 110.28 110.22 108.87 123.05 * * 86 ASP 86 1.329 1.230 1.536 1.543 1.476 123.51 116.62 120.93 110.56 111.64 109.66 122.42 * * 87 TRP 87 1.318 1.242 1.519 1.513 1.447 121.55 115.90 120.27 111.87 113.23 111.32 123.82 88 ALA 88 1.344 1.242 1.528 1.534 1.473 123.45 116.22 121.01 111.03 111.77 110.15 122.76 * * 89 ILE 89 1.319 1.230 1.527 1.562 1.451 121.67 115.84 121.05 110.34 108.88 111.83 123.08 90 GLN 90 1.309 1.242 1.520 1.530 1.446 122.46 116.01 121.40 110.13 110.13 109.34 122.58 * * 91 ALA 91 1.303 1.226 1.503 1.512 1.433 121.10 116.19 121.01 110.99 110.37 110.50 122.79 +* * * +* 92 MET 92 1.289 1.231 1.516 1.529 1.425 121.97 118.21 119.95 110.57 108.29 109.74 121.83 +** +* * * +** 93 PRO 93 1.332 1.239 1.541 1.527 1.452 123.75 116.08 121.09 110.17 112.55 102.07 122.80 94 THR 94 1.303 1.232 1.514 1.542 1.433 121.95 116.42 120.70 109.93 108.51 112.53 122.88 +* * +* 95 PHE 95 1.296 1.226 1.499 1.522 1.412 121.90 117.67 119.91 109.65 106.29 108.07 122.42 ** * ** +* * ** 96 MET 96 1.293 1.231 1.513 1.534 1.432 119.74 114.63 121.75 112.66 111.48 111.04 123.62 +** * * * +** 97 PHE 97 1.296 1.249 1.493 1.511 1.406 124.53 116.08 120.95 109.24 109.07 108.22 122.97 ** +* +** +* * +** 98 LEU 98 1.287 1.227 1.523 1.545 1.414 120.66 115.48 121.17 107.62 109.58 110.16 123.35 *** ** * *** 99 LYS 99 1.293 1.228 1.470 1.522 1.435 123.37 115.72 119.99 110.68 107.74 113.23 124.19 +** +** * * +* +** 100 GLU 100 1.319 1.227 1.534 1.508 1.452 123.16 115.90 121.14 110.86 112.37 109.91 122.94 * * 101 GLY 101 1.317 1.232 1.523 - 1.448 121.42 116.01 120.68 - 111.76 - 123.30 102 LYS 102 1.325 1.238 1.520 1.526 1.454 122.99 116.86 119.99 110.54 109.32 110.13 123.15 103 ILE 103 1.317 1.233 1.522 1.558 1.455 122.00 115.77 121.11 109.98 112.52 111.36 123.12 104 LEU 104 1.320 1.230 1.501 1.517 1.434 121.84 116.25 120.88 108.61 110.53 111.74 122.86 * * * Residue-by-residue listing for refined_10 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 105 ASP 105 1.318 1.222 1.493 1.530 1.449 120.57 115.31 121.12 107.36 111.22 112.26 123.57 +* * * +* 106 LYS 106 1.288 1.227 1.517 1.543 1.436 122.86 116.23 120.75 111.32 109.35 113.02 123.00 +** * * +** 107 VAL 107 1.297 1.234 1.512 1.559 1.444 122.34 115.76 120.72 109.65 108.85 111.48 123.48 ** ** 108 VAL 108 1.307 1.250 1.533 1.565 1.440 122.22 115.83 120.99 111.42 110.48 111.25 123.16 +* * +* 109 GLY 109 1.319 1.239 1.504 - 1.439 121.37 117.63 120.10 - 110.22 - 122.27 110 ALA 110 1.312 1.242 1.519 1.524 1.435 119.29 115.29 121.59 110.76 110.57 110.63 123.12 * * * * 111 LYS 111 1.307 1.216 1.490 1.518 1.419 123.25 116.17 120.39 110.81 108.78 110.69 123.44 +* +* ** ** 112 LYS 112 1.293 1.236 1.526 1.506 1.414 122.96 115.62 121.08 111.01 111.08 107.33 123.23 +** * ** +* +** 113 ASP 113 1.318 1.236 1.519 1.528 1.461 122.14 116.25 120.86 110.49 111.36 110.24 122.88 114 GLU 114 1.325 1.234 1.523 1.531 1.457 121.34 116.90 120.39 111.60 111.25 111.44 122.68 115 LEU 115 1.331 1.216 1.507 1.510 1.453 121.20 115.31 120.98 108.83 108.76 110.96 123.70 * * 116 GLN 116 1.322 1.230 1.519 1.529 1.476 122.73 115.95 120.91 109.48 111.13 111.01 123.11 117 SER 117 1.314 1.238 1.534 1.540 1.451 121.44 115.77 121.15 111.12 109.64 110.68 123.05 * * 118 THR 118 1.324 1.243 1.542 1.549 1.442 122.29 116.06 121.03 109.83 109.34 110.77 122.90 119 ILE 119 1.339 1.229 1.521 1.564 1.453 121.68 115.31 121.18 108.68 108.37 112.26 123.46 * * 120 ALA 120 1.318 1.221 1.529 1.515 1.452 123.03 116.97 120.18 111.20 111.96 110.63 122.85 121 LYS 121 1.327 1.229 1.521 1.508 1.462 122.35 114.79 121.78 108.64 109.45 109.28 123.43 * * 122 HIS 122 1.311 1.230 1.524 1.525 1.441 122.77 117.64 120.34 110.62 113.13 110.98 122.01 * * 123 LEU 123 1.314 1.237 1.516 1.513 1.411 121.18 114.96 121.67 112.43 112.25 110.66 123.34 * ** * ** 124 ALA 124 1.305 - 1.519 1.519 1.432 122.90 - - 110.62 109.86 109.68 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* * +** ** +*** +* ** * ** +* ** +* *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 11 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 119 1.264 1.344 1.312 .014 *4.6* * * C-N (Pro) 1.341 .016 4 1.332 1.374 1.351 .016 ** C-O C-O 1.231 .020 123 1.204 1.250 1.233 .008 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.470 1.556 1.520 .015 +** * CH2G*-C (Gly) 1.516 .018 5 1.495 1.535 1.511 .015 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.512 1.534 1.521 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.523 1.566 1.552 .012 CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.557 1.528 .014 ** * N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.383 1.476 1.441 .017 +*** NH1-CH2G* (Gly) 1.451 .016 5 1.427 1.471 1.446 .014 * * N-CH1E (Pro) 1.466 .015 4 1.452 1.476 1.469 .010 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 12 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 114 112.52 120.20 116.01 .99 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.01 118.95 117.20 1.02 * CH1E-C-N (Pro) 116.9 1.5 4 115.61 116.53 116.03 .33 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.46 124.94 123.03 .57 +* * O-C-N (Pro) 122.0 1.4 4 122.80 123.32 123.01 .22 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.52 125.15 122.21 1.16 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.65 122.60 121.69 .72 * C-N-CH1E (Pro) 122.6 5.0 4 121.55 123.75 122.70 .81 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.26 122.50 120.90 .58 * CH2G*-C-O (Gly) 120.8 2.1 5 119.78 120.82 120.34 .38 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.22 112.48 110.93 .51 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.47 111.92 110.09 1.05 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.36 114.37 110.53 1.30 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 106.29 114.13 110.19 1.49 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.74 114.77 111.83 1.80 N-CH1E-C (Pro) 111.8 2.5 4 111.35 113.95 112.46 .96 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 109.68 112.63 110.65 .66 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.29 114.00 111.22 1.10 +* * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.07 103.93 103.35 .76 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.33 114.34 110.42 1.62 +* ** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_10 Page 13 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 102 90.3% Residues in additional allowed regions [a,b,l,p] 11 9.7% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 113 90.3 83.8 10.0 .6 Inside b. Omega angle st dev 122 2.9 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 84 .8 .8 .2 .1 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 13 5.8 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 40 5.6 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 49 7.1 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 102 7.6 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 28 9.3 20.4 5.0 -2.2 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 90.3 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_10 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.16 Chi1-chi2 distribution -.06 Chi1 only .00 Chi3 & chi4 .26 Omega .08 ------ -.01 ===== Main-chain covalent forces:- Main-chain bond lengths -.02 Main-chain bond angles .44 ------ .25 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.